Header list of 1jr6.pdb file
Complete list - b 23 2 Bytes
HEADER HYDROLASE 10-AUG-01 1JR6
TITLE SOLUTION STRUCTURE OF AN ENGINEERED ARGININE-RICH SUBDOMAIN 2 OF THE
TITLE 2 HEPATITIS C VIRUS NS3 RNA HELICASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HELICASE NS3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ARGININE-RICH SUBDOMAIN 2;
COMPND 5 EC: 3.4.21.98;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS;
SOURCE 3 ORGANISM_TAXID: 11103;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PET28;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PNS3D2DELTA
KEYWDS ALPHA-BETA-ALPHA, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR D.LIU,D.F.WYSS,Y.S.WANG,J.J.GESELL
REVDAT 3 23-FEB-22 1JR6 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1JR6 1 VERSN
REVDAT 1 10-AUG-02 1JR6 0
JRNL AUTH D.LIU,Y.S.WANG,J.J.GESELL,D.F.WYSS
JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF AN ENGINEERED
JRNL TITL 2 ARGININE-RICH SUBDOMAIN 2 OF THE HEPATITIS C VIRUS NS3 RNA
JRNL TITL 3 HELICASE.
JRNL REF J.MOL.BIOL. V. 314 543 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11846566
JRNL DOI 10.1006/JMBI.2001.5146
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 98.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CALCULATION WAS BASED ON A TOTAL OF
REMARK 3 2397 INTERPROTON DISTANCE RESTRAINTS, 76 HYDROGEN BOND
REMARK 3 RESTRAINTS, 181 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1JR6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-01.
REMARK 100 THE DEPOSITION ID IS D_1000014094.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 75 MM KIPO4
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6 MM, U-15N,13C;; 0.6 MM, U
REMARK 210 -15N,13C;; 0.3 MM, U-15N
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 4.0, FELIX 97
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-25
REMARK 465 RES C SSSEQI
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O VAL A 113 H GLN A 117 1.53
REMARK 500 O ARG A 115 H ARG A 119 1.57
REMARK 500 O LEU A 30 H LYS A 34 1.58
REMARK 500 H ILE A 40 O VAL A 82 1.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 PRO A 6 -169.22 -69.12
REMARK 500 1 HIS A 7 79.44 175.68
REMARK 500 1 PHE A 23 96.26 -160.83
REMARK 500 1 PRO A 75 42.22 -92.58
REMARK 500 1 THR A 85 -126.09 -84.15
REMARK 500 1 ASP A 86 40.30 -101.41
REMARK 500 1 MET A 89 -150.52 53.71
REMARK 500 1 THR A 90 31.51 -150.62
REMARK 500 1 THR A 93 -154.78 -90.55
REMARK 500 1 ASN A 103 26.13 47.08
REMARK 500 1 ASP A 106 29.09 49.41
REMARK 500 1 GLN A 110 150.19 -49.21
REMARK 500 1 ARG A 121 -45.39 -164.70
REMARK 500 1 ALA A 134 96.75 54.24
REMARK 500 2 HIS A 7 76.55 170.71
REMARK 500 2 TYR A 24 81.66 -58.16
REMARK 500 2 SER A 72 -35.20 -132.63
REMARK 500 2 PRO A 75 39.16 -87.37
REMARK 500 2 THR A 76 46.88 -144.17
REMARK 500 2 ASN A 77 26.90 -142.26
REMARK 500 2 THR A 85 -136.02 -93.30
REMARK 500 2 ASP A 86 46.66 -86.38
REMARK 500 2 THR A 90 -118.89 33.92
REMARK 500 2 THR A 93 -154.41 -67.63
REMARK 500 2 ASN A 103 18.78 50.89
REMARK 500 2 GLN A 110 -177.16 -57.66
REMARK 500 2 ARG A 121 -43.52 -151.39
REMARK 500 3 HIS A 7 84.21 -176.55
REMARK 500 3 PRO A 8 83.21 -66.98
REMARK 500 3 ASN A 9 -36.99 -172.73
REMARK 500 3 PHE A 23 -169.57 -112.96
REMARK 500 3 TYR A 24 82.28 -59.44
REMARK 500 3 SER A 72 -39.28 -133.23
REMARK 500 3 PRO A 75 48.02 -84.46
REMARK 500 3 THR A 76 40.38 -148.10
REMARK 500 3 ASP A 86 32.50 -179.20
REMARK 500 3 MET A 89 -165.01 53.23
REMARK 500 3 THR A 93 -157.68 -80.38
REMARK 500 3 ASN A 103 13.42 57.24
REMARK 500 3 GLN A 110 154.85 -49.99
REMARK 500 3 ARG A 121 -46.45 -149.75
REMARK 500 4 HIS A 7 83.35 172.03
REMARK 500 4 PRO A 8 60.73 -66.16
REMARK 500 4 THR A 17 69.99 -68.55
REMARK 500 4 PHE A 23 93.70 -170.54
REMARK 500 4 TYR A 24 68.55 60.27
REMARK 500 4 SER A 72 -36.01 -134.28
REMARK 500 4 PRO A 75 46.82 -86.94
REMARK 500 4 THR A 85 -133.14 -91.34
REMARK 500 4 ASP A 86 43.30 -88.40
REMARK 500
REMARK 500 THIS ENTRY HAS 336 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 37 0.32 SIDE CHAIN
REMARK 500 1 ARG A 67 0.31 SIDE CHAIN
REMARK 500 1 ARG A 115 0.32 SIDE CHAIN
REMARK 500 1 ARG A 118 0.30 SIDE CHAIN
REMARK 500 1 ARG A 119 0.32 SIDE CHAIN
REMARK 500 1 ARG A 121 0.31 SIDE CHAIN
REMARK 500 1 ARG A 124 0.16 SIDE CHAIN
REMARK 500 1 ARG A 131 0.21 SIDE CHAIN
REMARK 500 1 ARG A 138 0.28 SIDE CHAIN
REMARK 500 2 ARG A 37 0.20 SIDE CHAIN
REMARK 500 2 ARG A 67 0.32 SIDE CHAIN
REMARK 500 2 ARG A 115 0.23 SIDE CHAIN
REMARK 500 2 ARG A 118 0.25 SIDE CHAIN
REMARK 500 2 ARG A 119 0.28 SIDE CHAIN
REMARK 500 2 ARG A 121 0.12 SIDE CHAIN
REMARK 500 2 ARG A 124 0.21 SIDE CHAIN
REMARK 500 2 ARG A 131 0.21 SIDE CHAIN
REMARK 500 2 ARG A 138 0.21 SIDE CHAIN
REMARK 500 3 ARG A 37 0.22 SIDE CHAIN
REMARK 500 3 ARG A 67 0.30 SIDE CHAIN
REMARK 500 3 ARG A 115 0.28 SIDE CHAIN
REMARK 500 3 ARG A 118 0.28 SIDE CHAIN
REMARK 500 3 ARG A 119 0.26 SIDE CHAIN
REMARK 500 3 ARG A 124 0.29 SIDE CHAIN
REMARK 500 3 ARG A 131 0.24 SIDE CHAIN
REMARK 500 3 ARG A 138 0.23 SIDE CHAIN
REMARK 500 4 ARG A 37 0.27 SIDE CHAIN
REMARK 500 4 ARG A 67 0.24 SIDE CHAIN
REMARK 500 4 ARG A 115 0.18 SIDE CHAIN
REMARK 500 4 ARG A 118 0.22 SIDE CHAIN
REMARK 500 4 ARG A 119 0.21 SIDE CHAIN
REMARK 500 4 ARG A 121 0.32 SIDE CHAIN
REMARK 500 4 ARG A 124 0.22 SIDE CHAIN
REMARK 500 4 ARG A 131 0.18 SIDE CHAIN
REMARK 500 4 ARG A 138 0.31 SIDE CHAIN
REMARK 500 5 ARG A 37 0.18 SIDE CHAIN
REMARK 500 5 ARG A 67 0.28 SIDE CHAIN
REMARK 500 5 ARG A 115 0.22 SIDE CHAIN
REMARK 500 5 ARG A 118 0.23 SIDE CHAIN
REMARK 500 5 ARG A 119 0.26 SIDE CHAIN
REMARK 500 5 ARG A 121 0.14 SIDE CHAIN
REMARK 500 5 ARG A 124 0.20 SIDE CHAIN
REMARK 500 5 ARG A 131 0.18 SIDE CHAIN
REMARK 500 5 ARG A 138 0.23 SIDE CHAIN
REMARK 500 6 ARG A 37 0.31 SIDE CHAIN
REMARK 500 6 ARG A 67 0.31 SIDE CHAIN
REMARK 500 6 ARG A 115 0.28 SIDE CHAIN
REMARK 500 6 ARG A 118 0.31 SIDE CHAIN
REMARK 500 6 ARG A 119 0.20 SIDE CHAIN
REMARK 500 6 ARG A 121 0.27 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 222 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JR6 A 1 138 UNP P27958 POLG_HCVH 1353 1507
SEQADV 1JR6 GLY A -3 UNP P27958 CLONING ARTIFACT
SEQADV 1JR6 SER A -2 UNP P27958 CLONING ARTIFACT
SEQADV 1JR6 HIS A -1 UNP P27958 CLONING ARTIFACT
SEQADV 1JR6 MET A 0 UNP P27958 CLONING ARTIFACT
SEQADV 1JR6 SER A 105 UNP P27958 SEE REMARK 999
SEQADV 1JR6 ASP A 106 UNP P27958 SEE REMARK 999
SEQADV 1JR6 GLY A 107 UNP P27958 SEE REMARK 999
SEQADV 1JR6 LYS A 108 UNP P27958 SEE REMARK 999
SEQADV 1JR6 A UNP P27958 CYS 1457 DELETION
SEQADV 1JR6 A UNP P27958 VAL 1458 DELETION
SEQADV 1JR6 A UNP P27958 THR 1459 DELETION
SEQADV 1JR6 A UNP P27958 GLN 1460 DELETION
SEQADV 1JR6 A UNP P27958 THR 1461 DELETION
SEQADV 1JR6 A UNP P27958 VAL 1462 DELETION
SEQADV 1JR6 A UNP P27958 ASP 1463 DELETION
SEQADV 1JR6 A UNP P27958 PHE 1464 DELETION
SEQADV 1JR6 A UNP P27958 SER 1465 DELETION
SEQADV 1JR6 A UNP P27958 LEU 1466 DELETION
SEQADV 1JR6 A UNP P27958 ASP 1467 DELETION
SEQADV 1JR6 A UNP P27958 PRO 1468 DELETION
SEQADV 1JR6 A UNP P27958 THR 1469 DELETION
SEQADV 1JR6 A UNP P27958 PHE 1470 DELETION
SEQADV 1JR6 A UNP P27958 THR 1471 DELETION
SEQADV 1JR6 A UNP P27958 ILE 1472 DELETION
SEQADV 1JR6 A UNP P27958 GLU 1473 DELETION
SEQADV 1JR6 A UNP P27958 THR 1474 DELETION
SEQADV 1JR6 A UNP P27958 ILE 1475 DELETION
SEQADV 1JR6 A UNP P27958 THR 1476 DELETION
SEQADV 1JR6 A UNP P27958 LEU 1477 DELETION
SEQRES 1 A 142 GLY SER HIS MET GLY SER VAL THR VAL PRO HIS PRO ASN
SEQRES 2 A 142 ILE GLU GLU VAL ALA LEU SER THR THR GLY GLU ILE PRO
SEQRES 3 A 142 PHE TYR GLY LYS ALA ILE PRO LEU GLU VAL ILE LYS GLY
SEQRES 4 A 142 GLY ARG HIS LEU ILE PHE CYS HIS SER LYS LYS LYS CYS
SEQRES 5 A 142 ASP GLU LEU ALA ALA LYS LEU VAL ALA LEU GLY ILE ASN
SEQRES 6 A 142 ALA VAL ALA TYR TYR ARG GLY LEU ASP VAL SER VAL ILE
SEQRES 7 A 142 PRO THR ASN GLY ASP VAL VAL VAL VAL ALA THR ASP ALA
SEQRES 8 A 142 LEU MET THR GLY PHE THR GLY ASP PHE ASP SER VAL ILE
SEQRES 9 A 142 ASP CYS ASN THR SER ASP GLY LYS PRO GLN ASP ALA VAL
SEQRES 10 A 142 SER ARG THR GLN ARG ARG GLY ARG THR GLY ARG GLY LYS
SEQRES 11 A 142 PRO GLY ILE TYR ARG PHE VAL ALA PRO GLY GLU ARG
HELIX 1 1 PRO A 29 LYS A 34 1 6
HELIX 2 2 SER A 44 GLY A 59 1 16
HELIX 3 3 ASP A 111 GLY A 120 1 10
SHEET 1 A 6 ILE A 10 ALA A 14 0
SHEET 2 A 6 GLY A 128 PHE A 132 1 O TYR A 130 N VAL A 13
SHEET 3 A 6 SER A 98 ASP A 101 1 N ASP A 101 O ARG A 131
SHEET 4 A 6 HIS A 38 PHE A 41 1 N LEU A 39 O SER A 98
SHEET 5 A 6 VAL A 80 ALA A 84 1 O VAL A 82 N ILE A 40
SHEET 6 A 6 ASN A 61 TYR A 65 1 N ASN A 61 O VAL A 81
SHEET 1 B 2 ILE A 21 PRO A 22 0
SHEET 2 B 2 ALA A 27 ILE A 28 -1 O ILE A 28 N ILE A 21
SHEET 1 C 2 THR A 104 SER A 105 0
SHEET 2 C 2 LYS A 108 PRO A 109 -1 O LYS A 108 N SER A 105
CRYST1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - b 23 2 Bytes